Other: PDZ Domain
The third PDZ domain from PSD-95.
Domain Binding and Function
PDZ domains bind to the C-terminal 4–5 residues of their target proteins, frequently transmembrane receptors or ion channels. These interactions can be of high affinity (nM Kd). The consensus binding sequence contains a hydrophobic residue, commonly Val or Ile, at the very C-terminus. Residues at the —2 and —3 positions are important in determining specificity. PDZ domains can also heterodimerize with PDZ domains of different proteins, potentially regulating intracellular signaling. In addition to engaging in protein-protein interactions, several PDZ domains including those of syntenin, CASK, Tiam1 and FAP are capable of binding to the phosphoinositide PIP2. PIP2-PDZ domain binding is thought to control the association of PDZ domain-containing proteins with the plasma membrane.
Structure Reference
- Doyle, D.A. et al. (1996) Cell 85(7), 1067–1076.
Examples of Domain Proteins
Binding Examples
| PDZ Domain Proteins | Binding Partners | Domain Binding Sites |
|---|---|---|
| Post-synaptic Density Protein 95 (PSD-95) | NMDA receptor B via PDZ1 and PDZ2 of PSD-95 | – IESDV-COOH |
| Post-synaptic Density Protein 95 (PSD-95) | Kvl1.4 Shaker-type K+ channel via PDZ1 and PDZ2 of PSD-95 | – VETDV-COOH |
| Post-synaptic Density Protein 95 (PSD-95) | Neural Nitric Oxide Synthase (nNOS) via PDZ2 | PDZ/PDZ interaction |
